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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pyruvate kinase and phosphoenolpyruvate carboxykinase activities were determined in microdissected freeze-dried liver cells from the periportal and pericentral area of the liver lobule. Pyruvate kinase activity was measured by a microfluorimetric procedure adapted to 20-200 ng tissue dry weight. In livers from fed rats, its activity was twice as high in the central zone as in the periportal cells; starvation reduced this gradient by decreasing central activities. Phosphoenolpyruvate carboxykinase activity was measured by a microradiochemical technique in 100-300 ng tissue dry weight. In livers from fed rats, this enzyme was nearly 3 times more active in the periportal cells than in the central area. Starvation increased this enzyme in both zones with a more pronounced change in the central cells. The results indicate a heterogeneous distribution of enzymes of carbohydrate metabolism in the liver lobule. Gluconegenesis seems to be localized preferentially in periportal hepatocytes, whereas the glycolytic enzyme was found to be more active in cells surrounding the pericentral liver cells.
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PMID:Liver cell heterogeneity. The distribution of pyruvate kinase and phosphoenolpyruvate carboxykinase (GTP) in the liver lobule of fed and starved rats. 101 1

Pathological conditions or nutrient deprivation in the heart cause an imbalance between rates of protein synthesis and degradation, often resulting in a severe depletion of cardiac protein. We used cultured neonatal rat heart cells, a model system exhibiting positive nitrogen balance, to examine the effects of 10 h of starvation on myocardial glucose and protein metabolism. Cellular capacity for glucose utilization was depressed after starvation, as evidenced by lower hexokinase and other glycolytic enzyme activities and a 21% decrease in glucose usage. A 21.0% decrease in protein synthetic rate and an increase in protein degradation rate combined to yield a 29.5% decrease in total cellular protein during starvation. Degradation rates increased 29.0, 46.7, and 59.6% in 2-, 24-, and 96-h prelabeled cells, respectively, indicating that lability increased with half-life of proteins. During refeeding of starved, cultured cells, at least three proteins were synthesized at a lower rate. At the same time, proteins with approximate molecular masses of 45, 84, 92, and 174 kDa exhibited increased synthesis.
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PMID:Protein metabolism during nutrient deprivation and refeeding of neonatal heart cells. 259 85

Six mutants lacking the glycolytic enzyme fructose 1,6-bisphosphate aldolase have been isolated in the yeast Saccharomyces cerevisiae by inositol starvation. The mutants grown on gluconeogenic substrates, such as glycerol or alcohol, and show growth inhibition by glucose and related sugars. The mutations are recessive, segregate as one gene in crosses, and fall in a single complementation group. All of the mutants synthesize an antigen cross-reacting to the antibody raised against yeast aldolase. The aldolase activity in various mutant alleles measured as fructose 1,6-bisphosphate cleavage is between 1 to 2% and as condensation of triose phosphates to fructose 1,6-bisphosphate is 2 to 5% that of the wild-type. The mutants accumulate fructose 1,6-bisphosphate from glucose during glycolysis and dihydroxyacetone phosphate during gluconeogenesis. This suggests that the aldolase activity is absent in vivo.
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PMID:Saccharomyces cerevisiae aldolase mutants. 638 92

Three unlinked genes, TDH1, TDH2 and TDH3, encode the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (triose-phosphate dehydrogenase; TDH) in the yeast Saccharomyces cerevisiae. We demonstrate that the synthesis of the three encoded TDH polypeptides (TDHa, TDHb and TDHc, respectively) is not co-ordinately regulated and that TDHa is only synthesised as cells enter stationary phase, due to glucose starvation, or in heat-shocked cells. Furthermore, the synthesis of TDHb, but not TDHc, is strongly repressed by a heat shock. Hence, the TDHa enzyme may play a cellular role, distinct from glycolysis, that is required by stressed cells.
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PMID:Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells. 787 59

Hepatocyte nuclear factors 3 (HNF-3) belong to an evolutionarily conserved family of transcription factors that are critical for diverse biological processes such as development, differentiation, and metabolism. To study the physiological role of HNF-3alpha, we generated mice that lack HNF-3alpha by homologous recombination in embryonic stem cells. Mice homozygous for a null mutation in the HNF-3alpha gene develop a complex phenotype that is characterized by abnormal feeding behavior, progressive starvation, persistent hypoglycemia, hypotriglyceridemia, wasting, and neonatal mortality between days 2 and 14. Hypoglycemia in HNF-3alpha-null mice leads to physiological counter-regulatory responses in glucocorticoid and growth hormone production and an inhibition of insulin secretion but fails to stimulate glucagon secretion. Glucagon-producing pancreatic alpha cells develop normally in HNF-3alpha-/- mice, but proglucagon mRNA levels are reduced 50%. Furthermore, the transcriptional levels of neuropeptide Y are also significantly reduced shortly after birth, implying a direct role of HNF-3alpha in the expression of these genes. In contrast, mRNA levels were increased in HNF-3 target genes phosphofructo-2-kinase/fructose-2,6-bisphophatase, insulin growth factor binding protein-1, and hexokinase I of HNF-3alpha-null mice. Mice lacking one or both HNF-3alpha alleles also show impaired insulin secretion and glucose intolerance after an intraperitoneal glucose challenge, indicating that pancreatic beta-cell function is also compromised. Our results indicate that HNF-3alpha plays a critical role in the regulation of glucose homeostasis and in pancreatic islet function.
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PMID:Impaired glucose homeostasis and neonatal mortality in hepatocyte nuclear factor 3alpha-deficient mice. 1046 78

This study evaluated the link between swimming endurance and condition of Atlantic cod Gadus morhua that had been fed or starved during the 16 weeks preceding the tests, and assessed whether muscle metabolic capacities explain such links. The condition factor [(somatic mass x fork length(-3))x100] of starved cod was 0.54+/-0.1 whereas that of fed cod was 0.81+/-0.1. In white and red muscle, we measured four glycolytic enzymes: phosphofructokinase (PFK), pyruvate kinase (PK), creatine kinase (CK) and lactate dehydrogenase (LDH), two mitochondrial enzymes: cytochrome c oxidase (CCO) and citrate synthase (CS), a biosynthetic enzyme, nucleoside diphosphate kinase (NDPK), glycogen and protein levels and water content. Muscle samples were taken at three positions along the length of the fish; starvation affected the metabolic capacities of white muscle more than those of red muscle. The levels of glycolytic enzymes and glycogen changed more in white than red muscle during starvation. Both in fed and starved cod, muscle metabolic capacities varied with position along the fish; starvation reduced this longitudinal variation more in white than red muscle. In white muscle of fed cod, the glycolytic enzyme levels increased from head to tail, while in starved cod this longitudinal variation disappeared. In red muscle mitochondrial enzyme levels were highest in the caudal sample, but fewer differences were found for glycolytic enzymes. Swimming endurance was markedly affected by fish condition, with starved fish swimming only 30% of the time (and distance) of fed fish. This endurance was closely linked with the number of burst-coast movements during the test and the activity of CCO and LDH in white muscle. The number of burst-coast movements was significantly linked with condition factor and PFK activity in caudal red muscle and gill arch mass. Our data indicated that cod use both glycolytic and oxidative capacities to support endurance swimming. Furthermore, swimming endurance is linked with the metabolic capacities of red and white muscle.
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PMID:Condition, prolonged swimming performance and muscle metabolic capacities of cod Gadus morhua. 1250 71

Atlantic cod, Gadus morhua, respond to starvation first by mobilising hepatic lipids, then muscle and hepatic glycogen and finally muscle proteins. The dual role of proteins as functional elements and energetic reserves should lead to a temporal hierarchy of mobilisation where the nature of a function dictates its conservation during starvation. We examined (1) whether lysosomal and anti-oxidant enzymes in liver and white muscle are spared during prolonged starvation, (2) whether the responses of these enzymes in muscle vary longitudinally. Hepatic contents of lysosomal proteases decreased with starvation, whereas those of catalase (CAT) increased and lysosomal enzymes of carbohydrate metabolism and glutathione S-transferase (GST) did not change. In white muscle, starvation decreased the specific activity of lysosomal enzymes of carbohydrate degradation and doubled that of cathepsin D (CaD). The activity of anti-oxidant enzymes and acid phosphatase in muscle was unchanged with starvation. In white muscle neither lysosomal enzymes nor anti-oxidant enzymes varied significantly with sampling position. In cod muscle, antioxidant enzymes, CaD and acid phosphatase are spared during a period of starvation that decreases lysosomal enzymes of carbohydrate metabolism and decreases glycolytic enzyme activities. In cod liver, the anti-oxidant enzymes, CAT and GST, were also spared during starvation.
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PMID:Metabolic priorities during starvation: enzyme sparing in liver and white muscle of Atlantic cod, Gadus morhua L. 1278 35

In Saccharomyces cerevisiae the HXK2 gene, which encodes the glycolytic enzyme hexokinase II, is involved in the regulatory mechanism known as 'glucose repression'. Its deletion leads to fully respiratory growth at high glucose concentrations where the wild type ferments profusely. Here we describe that deletion of the HXK2 gene resulted in a 75% reduction in fermentative capacity. Using regulation analysis we found that the fluxes through most glycolytic and fermentative enzymes were regulated cooperatively by changes in their capacities (Vmax) and by changes in the way they interacted with the rest of the metabolism. Glucose transport and phosphofructokinase were regulated purely at the metabolic level. The reduction of fermentative capacity in the mutant was accompanied by a remarkable resilience of the remaining capacity to nutrient starvation. After starvation, the fermentative capacity of the hxk2Delta mutant was similar to that of the wild type. Based on our results and previous reports, we suggest an inverse correlation between glucose repression and the resilience of fermentative capacity towards nutrient starvation. Only a limited number of glycolytic enzyme activities changed upon starvation of the hxk2Delta mutant and we discuss to what extent this could explain the stability of the fermentative capacity.
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PMID:Mixed and diverse metabolic and gene-expression regulation of the glycolytic and fermentative pathways in response to a HXK2 deletion in Saccharomyces cerevisiae. 1766 56

Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by 2-PG, which suggests that glucose metabolism controls the non-glycolytic function of enolase. Interestingly, glucose starvation drives enolase to accumulate within the nucleus, which in turn leads to the formation of additional enolase-E.histolytica DNMT2 homolog (Ehmeth) complex, and to a significant reduction of the tRNA(Asp) methylation in the parasite. The crucial role of enolase as a Dnmt2 inhibitor was also demonstrated in E.histolytica expressing a nuclear localization signal (NLS)-fused-enolase. These results establish enolase as the first Dnmt2 interacting protein, and highlight an unexpected role of a glycolytic enzyme in the modulation of Dnmt2 activity.
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PMID:A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity. 2017 8

Short-term starvation has been linked to in vivo protein degradation in liver of rainbow trout (Oncorhynchus mykiss). However, it is unclear whether this proposed increase in protein degradation is followed by programmed cell death (apoptosis) in liver of starved trout. A preliminary study in our laboratory revealed an isoform of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein that increased 4.5-fold in liver of starved trout. GAPDH is a glycolytic enzyme involved in other cellular functions, including apoptosis. Increased intracellular nitric oxide (NO) promotes nuclear translocation of GAPDH that is associated with increased apoptosis in mammals. If GAPDH protein is associated with apoptosis in rainbow trout, it could potentially be used as a biomarker of cellular stress in liver of teleost fish species. The purpose of this study was to determine whether increased GAPDH protein expression in liver of starved rainbow trout is associated with NO-induced apoptosis. Targeted proteomic analysis using multiple reaction monitoring (MRM) was used to determine the level of GAPDH in nuclear and cytoplasmic fractions and inducible nitric oxide synthase (iNOS) in cell lysates. Dot blot and DNA fragmentation analyses were conducted to evaluate protein S-nitrosylation and apoptosis, respectively. Results showed that cytoplasmic GAPDH was 3.4-fold higher in liver of starved versus fed rainbow trout but could not be detected in nuclear fractions. Starvation significantly reduced hepato-somatic index but had no effect on iNOS protein expression, protein S-nitrosylation, or apoptosis. Our results indicate that starvation promoted significant reduction in liver mass that was not associated with increased apoptosis or NO-induced stress and that greater GAPDH concentration in liver of starved rainbow trout was located primarily in the cytoplasm.
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PMID:Increased expression of GAPDH protein is not indicative of nitrosative stress or apoptosis in liver of starved rainbow trout (Oncorhynchus mykiss). 2164 98


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